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In this present investigation, an aqueous Basella alba leaves extract was used to synthesize AgNPs. The green synthesis approach is carried out in our work due to non-toxic, less cost, and ecofriendly methods. FTIR spectra are used to confirm the biomolecules present in B.alba leaves extract along with AgNPs and these compounds are responsible for Ag particle from micro to nanostructure. The FCC structure and crystalline nature of the AgNPs are analyzed with the help of XRD and TEM techniques respectively. DLS and Zeta potential techniques are carried out to find the size and stability of AgNPs respectively and UV is used to verify the presence of AgNPs in synthesized samples employing SPR peaks around 435 nm. The antioxidant studies expose eminent scavenging activity which ranges from 13.71% to maximum 67.88%. Green synthesized AgNPs possess well organized biological activities concerning antioxidant and antibacterial, which can be used in some biologically applications. • Biological technique is cost-efficient, capable of processing AgNPs at 60 °C. • Synthesized AgNPs were spherical in size and the size ranging from 18 to 35 nm. • The feasible biomolecules which are liable for the minimization of Ag+ ions. • Alkyl halides bond reported that the indicates association of alkanes. • AgNPs reported that proteins could bind to silver nanoparticles which are compatible. [ABSTRACT FROM AUTHOR]

Abstract Bacterial fatty acid synthesis (FAS) has been extensively studied as a potential target of antimicrobials. In FAS, FabD mediates transacylation of the malonyl group from malonyl-CoA to acyl-carrier protein (ACP). The mounting threat of nosocomial infection by multidrug-resistant Acinetobacter baumannii warrants a deeper understanding of its essential cellular mechanisms, which could lead to effective control of this highly competent pathogen. The molecular mechanisms involved in A. baumannii FAS are poorly understood, and recent research has suggested that Pseudomonas aeruginosa , a closely related nosocomial pathogen of A. baumannii , utilizes FAS to produce virulence factors. In this study, we solved the crystal structure of A. baumannii FabD (AbFabD) to provide a platform for the development of new antibacterial agents. Analysis of the structure of AbFabD confirmed the presence of highly conserved active site residues among bacterial homologs. Binding constants between AbFabD variants and A. baumannii ACP (AbACP) revealed critical conserved residues Lys195 and Lys200 involved in AbACP binding. Computational docking of a potential inhibitor, trifluoperazine, revealed a unique inhibitor-binding pocket near the substrate-binding site. The structural study presented herein will be useful for the structure-based design of potent AbFabD inhibitors. Highlights • We solved the crystal structure of A. baumannii FabD. • Highly conserved active site residues were present among bacterial homologs. • The critical conserved residues Lys195 and Lys200 were involved in AbACP binding. • There was a unique inhibitor binding pocket near the substrate binding site. • This study will be useful for structure-based design of AbFabD inhibitors. [ABSTRACT FROM AUTHOR]